O52792 · HMO_AMYOR
- Protein4-hydroxymandelate oxidase
- Genehmo
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids357 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
function
Catalyzes the oxidation of p-hydroxymandelate to p-hydroxybenzoylformate in the biosynthesis of L-(4-hydroxyphenyl)glycine and L-(3,5-dihydroxyphenyl)glycine, 2 non-proteinogenic amino acids occurring in the vancomycin group of antibiotics.
Catalytic activity
- (S)-4-hydroxymandelate + O2 = 4-hydroxyphenylglyoxylate + H2O2
Cofactor
Pathway
Antibiotic biosynthesis; vancomycin biosynthesis.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 126 | FMN (UniProtKB | ChEBI) | |||
Binding site | 128 | a 2-oxocarboxylate (UniProtKB | ChEBI) | |||
Binding site | 154 | FMN (UniProtKB | ChEBI) | |||
Binding site | 163 | a 2-oxocarboxylate (UniProtKB | ChEBI) | |||
Binding site | 228 | FMN (UniProtKB | ChEBI) | |||
Active site | 252 | Proton acceptor | |||
Binding site | 255 | a 2-oxocarboxylate (UniProtKB | ChEBI) | |||
Binding site | 283-287 | FMN (UniProtKB | ChEBI) | |||
Binding site | 306-307 | FMN (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | FMN binding | |
Molecular Function | L-lactate dehydrogenase activity | |
Molecular Function | oxidoreductase activity, acting on the CH-OH group of donors, oxygen as acceptor | |
Biological Process | vancomycin biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended name4-hydroxymandelate oxidase
- EC number
Gene names
Organism names
- Taxonomic lineageBacteria > Actinomycetota > Actinomycetes > Pseudonocardiales > Pseudonocardiaceae > Amycolatopsis
Accessions
- Primary accessionO52792
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Chain | PRO_0000430441 | 1-357 | 4-hydroxymandelate oxidase | ||
Interaction
Protein-protein interaction databases
Structure
Sequence
- Sequence statusComplete
- Length357
- Mass (Da)37,832
- Last updated1998-06-01 v1
- MD5 Checksum46D2EA1E201A933DDF5A6987CDFD0A30
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AJ223998 EMBL· GenBank· DDBJ | CAA11762.1 EMBL· GenBank· DDBJ | Genomic DNA |